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Division of Biomedical Engineering

Structure and metabolism of bovine aortic proteoglycans

Abstract

dc:description.abstract

Although a number of studies of arterial glycosaminoglycans have been carried out, there is comparatively little information available regarding the native state in which these glycosaminoglycans occur, namely covalently bound to protein to form proteoglycans. There are numerous factors that make arterial proteoglycans difficult to study, such as their relatively low concentration in the tissue a s compared to cartilaginous tissue, and their association with the fibrous elements of the matrix which make quantitative extraction difficult. In recent years reports of characterizations of arterial proteoglycans have appeared in the literature but they differ markedly in several respects. In order to minimize such variables, proteoglycans isolated from pure medial tissue of bovine aortas from different age groups have been studied. Isolation of these proteoglycans was carried out essentially as described for their counterparts from cartilage. Furthermore, proteoglycans have been isolated from a cultured clonal line of foetal bovine aortic medial smooth muscle cells and comparison s made between the two sources of material in terms of their proteoglycan monomer size and glycosaminoglycan composition.

Degree

thesis:*
Grantor dc:publisher.institution
Division of Biomedical Engineering
Year dc:date.issued
1983

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Murray, Eileen
Advisor dc:contributor.advisor
  • Scott-Burden, Timothy

Subjects

dc:subject × 2

Rights

Language dc:language.iso
en

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/11427/42831
OAI identifier oai:identifier
oai:open.uct.ac.za:11427/42831

Chain of custody

source
Harvested from
University of Cape Town
Base URL
open.uct.ac.za/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Murray, Eileen. Structure and metabolism of bovine aortic proteoglycans. Division of Biomedical Engineering, 1983. http://hdl.handle.net/11427/42831